Abstract:
Malate synthase G an important housekeeping enzyme of glyoxylate shunt in mycobacterium tuberculosis is involved in persistence. The pleotropicity in its function is enigmatic acting as adhesins, virulence factor and being extra cellularly secreted as well. The enzyme from bacterial sources is monomeric .We in our study provide concrete evidence for the first time for the existence of both active monomer and dimer population for mycobacterium malate synthase G. The investigation was carried out in pursuit of comparatively delineating the structure, activity, and stability properties of recombinant MtbMS monomer and dimer. The study attempts to unveil the basis of dimerization , induction of structural cooperativity and subsequent changes in the functional activity of these molecules using various biophysical techniques including fluoresence spectroscopy, circular dichroism ,size exclusion chromatography and bioinformatic tool. The findings clearly indicate that the formation of dimer is not an artifact or chance but a biological necessity
